Lip Flip Jersey City

This article needs additional citations for verification. Please help improve this article by adding citations to reliable sources. Unsourced material may be challenged and removed. Find sources: "Facial" – news · newspapers · books · scholar · JSTOR (March 2012) (Learn how and when to remove this message)

A facial is a family of skincare treatments for the face, including steam, exfoliation (physical and chemical), extraction, creams, lotions, facial masks, peels, and massage. They are normally performed in beauty salons but are also a common spa treatment. They are used for general skin health as well as for specific skin conditions. Types of facials include European facials,^[1] LED light therapy facials, hydrafacials, and mini-facials.

There are different kinds of masks (e.g., clay, cactus, cucumber) for different purposes: deep-cleansing, by penetrating the pores; healing acne scars or hyper-pigmentation; brightening, for a gradual illumination of the skin tone. Facial masks also help with anti-aging, acne, crows feet, under eye bags, sagging lids, dark circles, puffiness,^[2] and more. Some masks are designed to dry or solidify on the face, almost like plaster; others just remain wet.

Masks are removed by either rinsing the face with water, wiping off with a damp cloth, or peeling off of the face. The duration for wearing a mask varies with the type of mask and the manufacturer's usage instructions. The time can range from a few minutes to overnight. Those with sensitive skin are advised to first test out the mask on a small portion of the skin, in order to check for any irritations. Some facial masks are not suited to frequent use. A glycolic mask should not be used more frequently than once a month to avoid the risk of burning the skin.

Masks can be found anywhere from drugstores to department stores and can vary in consistency and form. Setting masks include: clay, which is a thicker consistency, and will draw out impurities (and sometimes, natural oils, too) from the pores; a cream, which stays damp to hydrate the skin; sheet-style, in which a paper mask is dampened with liquid to tone and moisturize the skin; and lastly, a hybrid/clay and cream form that includes small beads for removing dead surface skin cells. Non-setting facial masks include warm oil and paraffin wax masks. These different forms are made to suit different skin types (e.g., oily or dry), and different skincare goals or needs (e.g., moisturizing, cleansing, or exfoliating). Clay and mud masks suit oily and some "combination" skin types,^[3] while cream-based masks tend to suit dry and sensitive skin types. There are also peel-off masks, which are used to remove thin layers of dead skin cells and dirt.^[4]

• Spa treatment
• Acne
• Skin care

Glucagon-like peptide-1 (GLP-1) is a 30- or 31-amino-acid-long peptide hormone deriving from tissue-specific posttranslational processing of the proglucagon peptide. It is produced and secreted by intestinal enteroendocrine L-cells and certain neurons within the nucleus of the solitary tract in the brainstem upon food consumption. The initial product GLP-1 (1–37) is susceptible to amidation and proteolytic cleavage, which gives rise to the two truncated and equipotent biologically active forms, GLP-1 (7–36) amide and GLP-1 (7–37). Active GLP-1 protein secondary structure includes two α-helices from amino acid position 13–20 and 24–35 separated by a linker region.

Alongside glucose-dependent insulinotropic peptide (GIP), GLP-1 is an incretin; thus, it has the ability to decrease blood sugar levels in a glucose-dependent manner by enhancing the secretion of insulin. Beside the insulinotropic effects, GLP-1 has been associated with numerous regulatory and protective effects. Unlike GIP, the action of GLP-1 is preserved in patients with type 2 diabetes. Glucagon-like peptide-1 receptor agonists gained approval as drugs to treat diabetes and obesity starting in the 2000s.

Endogenous GLP-1 is rapidly degraded primarily by dipeptidyl peptidase-4 (DPP-4), as well as neutral endopeptidase 24.11 (NEP 24.11) and renal clearance, resulting in a half-life of approximately 2 minutes. Consequently, only 10–15% of GLP-1 reaches circulation intact, leading to fasting plasma levels of only 0–15 pmol/L. To overcome this, GLP-1 receptor agonists and DPP-4 inhibitors have been developed to increase GLP-1 activity. As opposed to common treatment agents such as insulin and sulphonylureas, GLP-1-based treatment has been associated with weight loss and a lower risk of hypoglycemia, two important considerations for patients with type 2 diabetes.

The proglucagon gene is expressed in several organs including the pancreas (α-cells of the islets of Langerhans), gut (intestinal enteroendocrine L-cells) and brain (caudal brainstem and hypothalamus). Pancreatic proglucagon gene expression is promoted upon fasting and hypoglycaemia induction and inhibited by insulin. Conversely, intestinal proglucagon gene expression is reduced during fasting and stimulated upon food consumption. In mammals, the transcription gives rise to identical mRNA in all three cell types, which is further translated to the 180 amino acid precursor called proglucagon. However, as a result of tissue-specific posttranslational processing mechanisms, different peptides are produced in the different cells.^[1][2]

In the pancreas (α-cells of the islets of Langerhans), proglucagon is cleaved by prohormone convertase (PC) 2 producing glicentin-related pancreatic peptide (GRPP), glucagon, intervening peptide-1 (IP-1) and major proglucagon fragment (MPGF).^[3]

In the gut and brain, proglucagon is catalysed by PC 1/3 giving rise to glicentin, which may be further processed to GRPP and oxyntomodulin, GLP-1, intervening peptide-2 (IP-2) and glucagon-like peptide-2 (GLP-2). Initially, GLP-1 was thought to correspond to proglucagon (72–108) suitable with the N-terminal of the MPGF, but sequencing experiments of endogenous GLP-1 revealed a structure corresponding to proglucagon (78–107) from which two discoveries were found. Firstly, the full-length GLP-1 (1–37) was found to be catalysed by endopeptidase to the biologically active GLP-1 (7–37). Secondly, the glycine corresponding to proglucagon (108) was found to serve as a substrate for amidation of the C-terminal arginine resulting in the equally potent GLP-1 (7–36) amide. In humans, almost all (>80%) secreted GLP-1 is amidated, whereas a considerable part remains GLP-1 (7–37) in other species.^[3][4]

GLP-1 is packaged in secretory granules and secreted into the hepatic portal system by the intestinal L-cells located primarily in the distal ileum and colon, but also found in the jejunum and duodenum. The L-cells are open-type triangular epithelial cells directly in contact with the lumen and neuro-vascular tissue and are accordingly stimulated by various nutrient, neural and endocrine factors.^[2]

GLP-1 is released in a biphasic pattern with an early phase after 10–15 minutes followed by a longer second phase after 30–60 minutes upon meal ingestion. As the majority of L-cells are located in the distal ileum and colon, the early phase is likely explained by neural signalling, gut peptides or neurotransmitters. Other evidence suggests the L-cells located in the proximal jejunum are sufficient to account for the early-phase secretion through direct contact with luminal nutrients. Less controversially, the second phase is likely caused by direct stimulation of L-cells by digested nutrients. The rate of gastric emptying is therefore an important aspect to consider, as it regulates the entry of nutrients into the small intestine where the direct stimulation occurs. One of the actions of GLP-1 is to inhibit gastric emptying, thus slowing down its own secretion (negative feedback) upon postprandial activation.^[1][2]

Fasting plasma concentrations of biologically active GLP-1 range between 0 and 15 pmol/L in humans and are increased 2- to 3-fold upon food consumption depending on meal size and nutrient composition. Individual nutrients, such as fatty acids, essential amino acids and dietary fibre have also been shown to stimulate GLP-1 secretion.

Sugars have been associated with various signalling pathways, which initiate depolarisation of the L-cell membrane causing an elevated concentration of cytosolic Ca²⁺, which in turn induces GLP-1 secretion. Fatty acids have been associated with the mobilisation of intracellular Ca²⁺ stores and subsequently release of Ca²⁺ into the cytosol. The mechanisms of protein-triggered GLP-1 secretion are less clear, but the amino acid proportion and composition appear important to the stimulatory effect.^[5]

Once secreted, GLP-1 is extremely susceptible to the catalytic activity of the proteolytic enzyme dipeptidyl peptidase-4 (DPP-4). Specifically, DPP-4 cleaves the peptide bond between Ala⁸-Glu⁹ resulting in the abundant GLP-1 (9–36) amide constituting 60–80% of total GLP-1 in circulation. DPP-4 is widely expressed in multiple tissues and cell types and exists in both a membrane-anchored and soluble circulating form. Notably, DPP-4 is expressed on the surface of endothelial cells, including those located directly adjacent to GLP-1 secretion sites.^[2] Consequently, less than 25% of secreted GLP-1 is estimated to leave the gut intact. Additionally, presumably due to the high concentration of DPP-4 found on hepatocytes, 40–50% of the remaining active GLP-1 is degraded across the liver. Thus, due to the activity of DPP-4 only 10–15% of secreted GLP-1 reaches circulation intact.^[3]

Neutral endopeptidase 24.11 (NEP 24.11) is a membrane-bound zinc metallopeptidase widely expressed in several tissues, but found in particularly high concentrations in the kidneys, which is also identified accountable for the rapid degradation of GLP-1. It primarily cleaves peptides at the N-terminal side of aromatic or hydrophobic amino acids and is estimated to contribute by up to 50% to GLP-1 degradation. However, the activity only becomes apparent once the degradation of DPP-4 has been prevented, as the majority of GLP-1 reaching the kidneys has already been processed by DPP-4. Similarly, renal clearance appear more significant for the elimination of already inactivated GLP-1.^[6]

The resulting half-life of active GLP-1 is approximately 2 minutes, which is however sufficient to activate GLP-1 receptors.

GLP-1 possesses several physiological properties making it (and its functional analogs) a subject of intensive investigation as a potential treatment of diabetes mellitus, as these actions induce long-term improvements along with the immediate effects.^{[need quotation to verify][7][8][9][10]} Although reduced GLP-1 secretion has previously been associated with attenuated incretin effect in patients with type 2 diabetes, further research indicates that GLP-1 secretion in patients with type 2 diabetes does not differ from healthy subjects.^[11]

The most noteworthy effect of GLP-1 is its ability to promote insulin secretion in a glucose-dependent manner. As GLP-1 binds to GLP-1 receptors expressed on pancreatic β cells, the receptors couple to G-protein subunits and activate adenylate cyclase, which increases the production of cAMP from ATP.^[3] Subsequently, activation of secondary pathways, including protein kinase A (PKA) and Epac2, alters cell ion channel activity, causing elevated levels of cytosolic Ca²⁺ that enhance exocytosis of insulin-containing granules. During the process, influx of glucose ensures sufficient ATP to sustain the stimulatory effect.^[3]

Additionally, GLP-1 ensures the β cell insulin stores are replenished to prevent exhaustion during secretion by promoting insulin gene transcription, mRNA stability and biosynthesis.^[2][12] GLP-1 also increases^[13] β cell mass by promoting proliferation and neogenesis while inhibiting apoptosis. As both type 1 and 2 diabetes are associated with reduction of functional β cells, this effect is desirable in diabetes treatment.^[12] An additional important effect of GLP-1, is inhibition of glucagon secretion at glucose levels above fasting levels. Critically, this does not affect the glucagon response to hypoglycemia as this effect is also glucose-dependent. The inhibitory effect is presumably mediated indirectly through somatostatin secretion, but a direct effect cannot be completely excluded.^[14][15]

In the brain, GLP-1 receptor activation has been linked with neurotrophic effects including neurogenesis^[16][17] and neuroprotective effects including reduced necrotic^[18] and apoptotic^[19][18] signaling, cell death,^[20][21] and dysfunctions.^[22] In the diseased brain, GLP-1 receptor agonist treatment is associated with protection against a range of experimental disease models such as Parkinson's disease,^[23][17] Alzheimer's disease,^[24][25] stroke,^[23] traumatic brain injury,^[13][18] and multiple sclerosis.^[26] In accordance with the expression of GLP-1 receptor on brainstem and hypothalamus, GLP-1 has been shown to promote satiety and thereby reduce food and water intake. Consequently, diabetic subjects treated with GLP-1 receptor agonists often experience weight loss as opposed to the weight gain commonly induced with other treatment agents.^[2][15]

In the stomach, GLP-1 inhibits gastric emptying, acid secretion and motility, which collectively decrease appetite. By decelerating gastric emptying GLP-1 reduces postprandial glucose excursion which is another attractive property regarding diabetes treatment. However, these gastrointestinal activities are also the reason why subjects treated with GLP-1-based agents occasionally experience nausea.^[14]

GLP-1 has also shown signs of carrying out protective and regulatory effects in numerous other tissues, including heart, tongue, adipose, muscles, bones, kidneys, liver and lungs.^{[citation needed]}

In the early 1980s, Richard Goodman and P. Kay Lund were postdoctoral researchers working in Joel Habener's laboratory at Massachusetts General Hospital.^[27] Starting in 1979, Goodman harvested DNA from American anglerfish islet cells and spliced the DNA into bacteria to find the gene for somatostatin; Lund then joined the Habener laboratory and used Goodman's bacteria to identify the gene for glucagon.^[27] In 1982, they published their discovery that the gene for proglucagon actually codes for three peptides, namely glucagon and two novel peptides.^[27] Those two novel peptides were later isolated, identified, and investigated by other researchers, and are now known as glucagon-like peptide-1 and glucagon-like peptide-2.^[27]

In the 1980s, Svetlana Mojsov worked on the identification of GLP-1 at Massachusetts General Hospital, where she was head of a peptide synthesis facility.^[28] To try to identify whether a specific fragment of GLP-q was an incretin, Mojsov created an incretin-antibody and developed ways to track its presence. She identified that a stretch of 31 amino acids in the GLP-1 was an incretin.^[29][30] Mojsov and her collaborators Daniel J. Drucker and Habener showed that small quantities of laboratory-synthesized GLP-1 could trigger insulin.^[31][32][33]

Mojsov fought to have her name included in patents, with Mass General eventually agreeing to amend four patents to include her name. She received her one-third of drug royalties for one year.^[28]

The discovery of GLP-1's extremely short half-life meant that it was impossible to develop into a drug.^[34][35] This caused diabetes research to shift towards other therapeutic options such as targeting the GLP-1 receptor, which then led to the development of GLP-1 receptor agonists.^[34][35]

• Glucagon
• Glucagon-like peptide-1 receptor
• Glucagon-like peptide-2
• Type 2 diabetes
• GLP-1 receptor agonists — albiglutide, dulaglutide, exenatide, liraglutide, lixisenatide, tirzepatide and semaglutide, the latter of which is marketed under the brands Ozempic, Rybelsus and Wegovy.
• Dipeptidyl peptidase-4
• Gastric inhibitory polypeptide

• Banting and Best Diabetes Centre at UT glp1
• Glucagon-Like+Peptide+1 at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
• Insulin release pathways

An injection (often and usually referred to as a "shot" in US English, a "jab" in UK English, or a "jag" in Scottish English and Scots) is the act of administering a liquid, especially a drug, into a person's body using a needle (usually a hypodermic needle) and a syringe.^[1] An injection is considered a form of parenteral drug administration; it does not involve absorption in the digestive tract. This allows the medication to be absorbed more rapidly and avoid the first pass effect. There are many types of injection, which are generally named after the body tissue the injection is administered into. This includes common injections such as subcutaneous, intramuscular, and intravenous injections, as well as less common injections such as epidural, intraperitoneal, intraosseous, intracardiac, intraarticular, and intracavernous injections.

Injections are among the most common health care procedures, with at least 16 billion administered in developing and transitional countries each year.^[2] Of these, 95% are used in curative care or as treatment for a condition, 3% are to provide immunizations/vaccinations, and the rest are used for other purposes, including blood transfusions.^[2] The term injection is sometimes used synonymously with inoculation, but injection does not only refer to the act of inoculation. Injections generally administer a medication as a bolus (or one-time) dose, but can also be used for continuous drug administration.^[3] After injection, a medication may be designed to be released slowly, called a depot injection, which can produce long-lasting effects.

An injection necessarily causes a small puncture wound to the body, and thus may cause localized pain or infection. The occurrence of these side effects varies based on injection location, the substance injected, needle gauge, procedure, and individual sensitivity. Rarely, more serious side effects including gangrene, sepsis, and nerve damage may occur. Fear of needles, also called needle phobia, is also common and may result in anxiety and fainting before, during, or after an injection. To prevent the localized pain that occurs with injections the injection site may be numbed or cooled before injection and the person receiving the injection may be distracted by a conversation or similar means. To reduce the risk of infection from injections, proper aseptic technique should be followed to clean the injection site before administration. If needles or syringes are reused between people, or if an accidental needlestick occurs, there is a risk of transmission of bloodborne diseases such as HIV and hepatitis.

Unsafe injection practices contribute to the spread of bloodborne diseases, especially in less-developed countries. To combat this, safety syringes exist which contain features to prevent accidental needlestick injury and reuse of the syringe after it is used once. Furthermore, recreational drug users who use injections to administer the drugs commonly share or reuse needles after an injection. This has led to the development of needle exchange programs and safe injection sites as a public health measure, which may provide new, sterile syringes and needles to discourage the reuse of syringes and needles. Used needles should ideally be placed in a purpose-made sharps container which is safe and resistant to puncture. Some locations provide free disposal programs for such containers for their citizens.

Injections are classified in multiple ways, including the type of tissue being injected into, the location in the body the injection is designed to produce effects, and the duration of the effects. Regardless of classification, injections require a puncture to be made, thus requiring sterile environments and procedures to minimize the risk of introducing pathogens into the body. All injections are considered forms of parenteral administration, which avoids the first pass metabolism which would potentially affect a medication absorbed through the gastrointestinal tract.

Many injections are designed to administer a medication which has an effect throughout the body. Systemic injections may be used when a person cannot take medicine by mouth, or when the medication itself would not be absorbed into circulation from the gastrointestinal tract. Medications administered via a systemic injection will enter into blood circulation, either directly or indirectly, and thus will have an effect on the entire body.